Biochemical Activities of Pediococcus pentosaceus isolates of Dairy Origin

Abstract

Eighty-three strains of pediococci were isolated from raw goat milk and Feta and Kaseri cheese and were characterized as Pediococcus pentosaceus (75 strains) and P. pentosaceus subspecies intermedins (8 strains). The hydrolases of 49 P. pentosaceus strains were examined with the API ZYM system. Leucine aminopeptidase and valine aminopeptidase were the strongest activities found (means 4.98 and 4.92, respectively, on a five-point color intensity scale) and were found in all strains. Activities of β-galactosidase and N-acetyl-β-glucosamidase were found in 96 and 92% of the strains, respectively, and were slightly weaker (mean activities of 4.61 and 4.17, respectively). Considerably lower were the activities of β-glucosidase (mean 2.99) and phosphoamidase (mean 1.55) and were detected in 98 and 55% of the strains, respectively. Very weak (<1) esterase, esterase:lipase, lipase, phosphoamidase, cystine aminopeptidase, or acid phosphatase activities were found in various numbers of strains. These results give information about the biochemical activities of P. pentosaceus species found in milk and cheese. © 1989, American Dairy Science Association. All rights reserved.